title: Bisucaberin biosynthesis: an adenylating domain of the BibC multi-enzyme catalyzes cyclodimerization of N-hydroxy-N-succinylcadaverine.
abstract: The bisucaberin biosynthetic gene cluster has been identified in Vibrio salmonicida and a domain from within the BibC multienzyme encoded by the cluster has been shown to catalyse ATP-dependent dimerisation and macrocyclisation of N-hydroxy-N-succinylcadaverine to form bisucaberin.
authors.affiliation: Department of Chemistry, University of Warwick, Coventry, UKCV4 7AL.
authors.forename: Nadia
authors.initials: N
authors.lastname: Kadi
authors.forename: Lijiang
authors.initials: L
authors.lastname: Song
authors.forename: Gregory L
authors.initials: GL
authors.lastname: Challis
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry*; D002103:Cadaverine / Q000031:analogs & derivatives* / Q000737:chemistry; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D003500:Cyclization; D019281:Dimerization; D010456:Peptides, Cyclic / Q000096:biosynthesis*; D021241:Spectrometry, Mass, Electrospray Ionization; D014733:Vibrio / Q000201:enzymology*
chemical_list: C533828:N-hydroxy-N-succinylcadaverine; D010456:Peptides, Cyclic; C054842:bisucaberin; D000255:Adenosine Triphosphate; D002103:Cadaverine